Difference between revisions of "RsiV"
Line 86: | Line 86: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
+ | ** upon exposure to lysozyme, the extracellular domain of [[RsiV]] is cleaved off by an unknown protease, subsequently the N-terminal part of the protein is subject to intramemrane proteolysis by [[RasP]] {{PubMed|23687273}} | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
− | ** [[SigV]]-[[RsiV]] | + | ** [[SigV]]-[[RsiV]], this interaction inhibits the activity of [[SigV]] {{PubMed|23687273}} |
− | ** [[RasP]]-[[RsiV]] {{PubMed|23687273}} | + | ** [[RasP]]-[[RsiV]], degradation of [[RsiV]] {{PubMed|23687273}} |
* '''[[Localization]]:''' | * '''[[Localization]]:''' |
Revision as of 16:38, 27 May 2013
- Description: anti-sigma factor to SigV
Gene name | rsiV |
Synonyms | yrhM |
Essential | no |
Product | anti-sigma factor to SigV |
Function | control of SigV activity |
Gene expression levels in SubtiExpress: rsiV | |
Interactions involving this protein in SubtInteract: RsiV | |
MW, pI | 32 kDa, 5.833 |
Gene length, protein length | 855 bp, 285 aa |
Immediate neighbours | sigV, oatA |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
sigma factors and their control, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU27130
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- membrane PubMed
Database entries
- Structure:
- UniProt: O05403
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Jessica L Hastie, Kyle B Williams, Craig D Ellermeier
The activity of σV, an extracytoplasmic function σ factor of Bacillus subtilis, is controlled by regulated proteolysis of the anti-σ factor RsiV.
J Bacteriol: 2013, 195(14);3135-44
[PubMed:23687273]
[WorldCat.org]
[DOI]
(I p)
Yun Luo, Kei Asai, Yoshito Sadaie, John D Helmann
Transcriptomic and phenotypic characterization of a Bacillus subtilis strain without extracytoplasmic function σ factors.
J Bacteriol: 2010, 192(21);5736-45
[PubMed:20817771]
[WorldCat.org]
[DOI]
(I p)
Stephan Zellmeier, Claudia Hofmann, Sylvia Thomas, Thomas Wiegert, Wolfgang Schumann
Identification of sigma(V)-dependent genes of Bacillus subtilis.
FEMS Microbiol Lett: 2005, 253(2);221-9
[PubMed:16274938]
[WorldCat.org]
[DOI]
(P p)
Mika Yoshimura, Kei Asai, Yoshito Sadaie, Hirofumi Yoshikawa
Interaction of Bacillus subtilis extracytoplasmic function (ECF) sigma factors with the N-terminal regions of their potential anti-sigma factors.
Microbiology (Reading): 2004, 150(Pt 3);591-599
[PubMed:14993308]
[WorldCat.org]
[DOI]
(P p)